Isolation, purification, and characterization of L-glutamate oxidase from Streptomyces sp. 18G

An extracellular L-glutamate oxidase (GLOD) was purified from soil-isolated Streptomyces sp 18G. The enzyme had a molecular weight of approximately 120,000 and consisted of two identical subunits, each with a molecular weight of 61,000. The isoelectric point was pH 8.5 and the enzyme had an optimal...

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Autores principales:	Wachiratianchai,Supawadee, Bhumiratana,Amaret, Udomsopagit,Suchat
Lenguaje:	English
Publicado:	Pontificia Universidad Católica de Valparaíso 2004
Acceso en línea:	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582004000300009
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spelling	oai:scielo:S0717-345820040003000092005-05-31Isolation, purification, and characterization of L-glutamate oxidase from Streptomyces sp. 18GWachiratianchai,SupawadeeBhumiratana,AmaretUdomsopagit,Suchat An extracellular L-glutamate oxidase (GLOD) was purified from soil-isolated Streptomyces sp 18G. The enzyme had a molecular weight of approximately 120,000 and consisted of two identical subunits, each with a molecular weight of 61,000. The isoelectric point was pH 8.5 and the enzyme had an optimal pH between 7.0-7.4. GLOD showed the maximum activity at 37ºC. The GLOD activity was stable at pH ranging from 6.5 to 7.0 for 1 hr. Among 21 amino acids tested for substrate specificity, L-glutamate was almost exclusively oxidized. D-glutamate and L-aspartate were oxidized but only to extents of 0.79% and 0.53%, respectively.info:eu-repo/semantics/openAccessPontificia Universidad Católica de ValparaísoElectronic Journal of Biotechnology v.7 n.3 20042004-12-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582004000300009en
institution	Scielo Chile
collection	Scielo Chile
language	English
description	An extracellular L-glutamate oxidase (GLOD) was purified from soil-isolated Streptomyces sp 18G. The enzyme had a molecular weight of approximately 120,000 and consisted of two identical subunits, each with a molecular weight of 61,000. The isoelectric point was pH 8.5 and the enzyme had an optimal pH between 7.0-7.4. GLOD showed the maximum activity at 37ºC. The GLOD activity was stable at pH ranging from 6.5 to 7.0 for 1 hr. Among 21 amino acids tested for substrate specificity, L-glutamate was almost exclusively oxidized. D-glutamate and L-aspartate were oxidized but only to extents of 0.79% and 0.53%, respectively.
author	Wachiratianchai,Supawadee Bhumiratana,Amaret Udomsopagit,Suchat
spellingShingle	Wachiratianchai,Supawadee Bhumiratana,Amaret Udomsopagit,Suchat Isolation, purification, and characterization of L-glutamate oxidase from Streptomyces sp. 18G
author_facet	Wachiratianchai,Supawadee Bhumiratana,Amaret Udomsopagit,Suchat
author_sort	Wachiratianchai,Supawadee
title	Isolation, purification, and characterization of L-glutamate oxidase from Streptomyces sp. 18G
title_short	Isolation, purification, and characterization of L-glutamate oxidase from Streptomyces sp. 18G
title_full	Isolation, purification, and characterization of L-glutamate oxidase from Streptomyces sp. 18G
title_fullStr	Isolation, purification, and characterization of L-glutamate oxidase from Streptomyces sp. 18G
title_full_unstemmed	Isolation, purification, and characterization of L-glutamate oxidase from Streptomyces sp. 18G
title_sort	isolation, purification, and characterization of l-glutamate oxidase from streptomyces sp. 18g
publisher	Pontificia Universidad Católica de Valparaíso
publishDate	2004
url	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582004000300009
work_keys_str_mv	AT wachiratianchaisupawadee isolationpurificationandcharacterizationoflglutamateoxidasefromstreptomycessp18g AT bhumiratanaamaret isolationpurificationandcharacterizationoflglutamateoxidasefromstreptomycessp18g AT udomsopagitsuchat isolationpurificationandcharacterizationoflglutamateoxidasefromstreptomycessp18g
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Isolation, purification, and characterization of L-glutamate oxidase from Streptomyces sp. 18G

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